Zobrazeno 1 - 7
of 7
pro vyhledávání: '"S. A. Darst"'
Autor:
Alex Goldfarb, E. Severinova, S. A. Darst, Arkady Mustaev, David Fenyö, B. T. Chait, Konstantine Severinov
Publikováno v:
Journal of Biological Chemistry. 269:20826-20828
Ribonucleotide analogs bound in the initiating site of Escherichia coli RNA polymerase holoenzyme in open promoter complexes were cross-linked to the beta and sigma 70 subunits. Using limited proteolysis and chemical degradation, the cross-link site
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::82d9ef412f61de4593708a106db4709b
https://doi.org/10.1016/s0021-9258(17)31896-3
https://doi.org/10.1016/s0021-9258(17)31896-3
Autor:
E A, Campbell, S A, Darst
Publikováno v:
Journal of molecular biology. 300(1)
The developmental regulatory protein sigma(F) of Bacillus subtilis, a member of the sigma(70)-family of bacterial RNA polymerase sigma factors, is negatively regulated by the anti-sigma factor SpoIIAB, which binds to sigma(F), sequestering it in an i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1a6337540d5354ed7c76246c638ba43d
https://pubmed.ncbi.nlm.nih.gov/10864495
https://pubmed.ncbi.nlm.nih.gov/10864495
Publikováno v:
Journal of molecular biology. 279(1)
The 10 kDa bacteriophage T4 antisigma protein AsiA binds the Escherichia coli RNA polymerase promoter specificity subunit, sigma 70, with high affinity and inhibits its transcription activity. AsiA binds to sigma 70 primarily through an interaction w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::588eedfb73d6943ffda77dc07e09a6c5
https://pubmed.ncbi.nlm.nih.gov/9636696
https://pubmed.ncbi.nlm.nih.gov/9636696
Autor:
E, Severinova, K, Severinov, D, Fenyö, M, Marr, E N, Brody, J W, Roberts, B T, Chait, S A, Darst
Publikováno v:
Journal of molecular biology. 263(5)
We used limited trypsin digestion to determine the domain organization of the Escherichia coli RNA polymerase sigma 70 subunit. Trypsin-resistant fragments containing sigma 70 conserved region 2 (sigma 70(2)), and carboxy-terminal fragments containin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::ea8e21f2575abcf61b94d19865b86e22
https://pubmed.ncbi.nlm.nih.gov/8947564
https://pubmed.ncbi.nlm.nih.gov/8947564
Publikováno v:
The Journal of biological chemistry. 271(44)
The beta and beta' subunits of Escherichia coli DNA-dependent RNA polymerase are highly conserved throughout eubacterial and eukaryotic kingdoms. However, in some archaebacteria and chloroplasts, the corresponding sequences are "split" into smaller p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::08297506c72fc124711f95b16ffbc1f7
https://pubmed.ncbi.nlm.nih.gov/8910400
https://pubmed.ncbi.nlm.nih.gov/8910400
Publikováno v:
The Journal of biological chemistry. 269(33)
Ribonucleotide analogs bound in the initiating site of Escherichia coli RNA polymerase holoenzyme in open promoter complexes were cross-linked to the beta and sigma 70 subunits. Using limited proteolysis and chemical degradation, the cross-link site
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f4fc358ee82e5faf5a194882dfc2b06e
https://pubmed.ncbi.nlm.nih.gov/8063697
https://pubmed.ncbi.nlm.nih.gov/8063697
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 1990, 216 (2), pp.353-62
Journal of Molecular Biology, Elsevier, 1990, 216 (2), pp.353-62
Two-dimensional crystals of yeast RNA polymerase A (I) were obtained by interaction with positively charged lipid layers. The analysis of single molecular images of lipid-bound RNA polymerases showed that the enzyme was preferentially oriented by the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::93bae9d0c3bf452cb6ed7b808cb0edba
https://hal.archives-ouvertes.fr/hal-00174068
https://hal.archives-ouvertes.fr/hal-00174068
